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UniProtKB/Swiss-Prot entry Q5RC63


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PRDX2_PONAB
Primary accession number Q5RC63
Secondary accession numbers None
Integrated into Swiss-Prot on October 31, 2006
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 32)
Name and origin of the protein
Protein name Peroxiredoxin-2
Synonym EC 1.11.1.15
Gene name
Name: PRDX2
From
Pongo abelii (Sumatran orangutan) [TaxID: 9601] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Pongo.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
The German cDNA consortium;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
Comments
  • FUNCTION: Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2) (By similarity).
  • CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
  • SUBUNIT: Homodimer; disulfide-linked, upon oxidation. Interacts with TIPIN (By similarity).
  • SUBCELLULAR LOCATION: Cytoplasm (By similarity).
  • MISCELLANEOUS: The active site is the redox-active Cys-51 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-173-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin (By similarity).
  • MISCELLANEOUS: Inactivated upon oxidative stress by overoxidation of Cys-51 to Cys-SO(2)H and Cys-SO(3)H. Cys-SO(2)H is retroreduced to Cys-SOH after removal of H(2)O(2), while Cys-SO(3)H may be irreversibly oxidized (By similarity).
  • SIMILARITY: Belongs to the ahpC/TSA family.
  • SIMILARITY: Contains 1 thioredoxin domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CR858417; CAH90647.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
SMR Q5RC63; 2-169, 3-170.
ModBase Q5RC63.
Protein family/group databases
PeroxiBase 4552; Ppy2CysPrx02.
Family and domain databases
InterPro IPR000866; AhpC-TSA.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 1.
Pfam PF00578; AhpC-TSA; 1.
Pfam graphical view of domain structure.
PROSITE PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q5RC63.
Phylogenomic databases
HOVERGEN Q5RC63; -.
Other
ProtoNet Q5RC63.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Antioxidant; Cytoplasm; Oxidoreductase; Peroxidase; Redox-active center.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   177  176     Peroxiredoxin-2. PRO_0000256857
DOMAIN   6   164  159     Thioredoxin. 
ACT_SITE   51    51        Cysteine sulfenic acid (-SOH) intermediate (By similarity). 
MOD_RES   2     2        N-acetylalanine (By similarity). 
DISULFID   51    51        Interchain (with C-173); in linked form (By similarity). 
DISULFID   173   173        Interchain (with C-51); in linked form (By similarity). 
Sequence information
Length: 177 AA [This is the length of the unprocessed precursor] Molecular weight: 19430 Da [This is the MW of the unprocessed precursor] CRC64: 6D95970252096370 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MASGNARIGK PAPDFKATAV VDGAFKEVKL SDYKGKYVVL FFYPLDFTFV CPTEIIAFSN 

        70         80         90        100        110        120 
RAEDFHKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTRR LSEDYGVLKT 

       130        140        150        160        170 
DEGIAYRGLF IIDGKGVLRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE GPCFASP 

Q5RC63 in FASTA format

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